BMRB Entry 6834

Title:
Solution Structure of the hSet2/HYPB SRI domain
Deposition date:
2005-09-21
Original release date:
2007-02-05
Authors:
Li, M.; Phatnani, H.; Greenleaf, A.; Zhou, P.
Citation:

Citation: Li, M.; Phatnani, H.; Greenleaf, A.; Zhou, P.. "NMR assignment of the SRI domain of human Set2/HYPB."  J. Biomol. NMR 36, 5-5 (2006).
PubMed: 16435090

Assembly members:

Assembly members:
the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1: GSHMTAEADTSSELAKKSKE VFRKEMSQFIVQCLNPYRKP DCKVGRITTTEDFKHLARKL THGVMNKELKYCKNPEDLEC NENVKHKTKEYIKKYMQKFG AVYKPKEDTELE

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts110
1H chemical shifts756

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Huntingtin interacting protein B1

Entities:

Entity 1, Huntingtin interacting protein B 112 residues - Formula weight is not available

1   GLYSERHISMETTHRALAGLUALAASPTHR
2   SERSERGLULEUALALYSLYSSERLYSGLU
3   VALPHEARGLYSGLUMETSERGLNPHEILE
4   VALGLNCYSLEUASNPROTYRARGLYSPRO
5   ASPCYSLYSVALGLYARGILETHRTHRTHR
6   GLUASPPHELYSHISLEUALAARGLYSLEU
7   THRHISGLYVALMETASNLYSGLULEULYS
8   TYRCYSLYSASNPROGLUASPLEUGLUCYS
9   ASNGLUASNVALLYSHISLYSTHRLYSGLU
10   TYRILELYSLYSTYRMETGLNLYSPHEGLY
11   ALAVALTYRLYSPROLYSGLUASPTHRGLU
12   LEUGLU

Samples:

sample_1: the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1, [U-15N], 2.0 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_2: the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1, [U-95% 13C; U-98% 15N], 2.0 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_3: the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1, [U-15N]-Lys, 2.0 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_4: the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1, [U-95% 13C; U-98% 15N], 2.0 mM; KCl 100 mM; D2O 100%

sample_5: the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1 2.0 mM; KCl 100 mM; D2O 100%

sample_6: the Set2-Rpb1-Interacting domain of Huntingtin interacting protein B isoform 1, [U-10% 13C], 2.0 mM; KCl 100 mM; D2O 100%

sample_cond_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYnot availablenot availablenot available
3D_13C-separated_NOESYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
HNCAnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
HN(CA)CBnot availablenot availablenot available
HN(COCA)CBnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCA-Jnot availablenot availablenot available
4D HC(CCO)NH-TOCSYnot availablenot availablenot available
15N-HSQCnot availablenot availablenot available
high-resolution 13C-HSQCnot availablenot availablenot available
RDC experiment in phagenot availablenot availablenot available

Software:

NMRPipe - processing

XEASY v1.2 - data analysis

DYANA v1.5 - structure solution

CYANA v2.0 - structure solution

X-PLOR NIH v2.9.7 - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB21823 BAD32524 BAG10485
EMBL CAC28349 CAD28492
GB AAC26194 AAH31601 AAH59049 AAH90954 AAI17163
REF NP_001074809 NP_001101659 NP_054878 XP_001113652 XP_001375978
SP E9Q5F9 Q9BYW2
TPG DAA16805
AlphaFold E9Q5F9 Q9BYW2

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks